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| ==Crystal structure of Galectin 8 with NDP52 peptide== | | ==Crystal structure of Galectin 8 with NDP52 peptide== |
| <StructureSection load='4han' size='340' side='right' caption='[[4han]], [[Resolution|resolution]] 2.55Å' scene=''> | | <StructureSection load='4han' size='340' side='right'caption='[[4han]], [[Resolution|resolution]] 2.55Å' scene=''> |
| == Structural highlights == | | == Structural highlights == |
| <table><tr><td colspan='2'>[[4han]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4HAN OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4HAN FirstGlance]. <br> | | <table><tr><td colspan='2'>[[4han]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4HAN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4HAN FirstGlance]. <br> |
| </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene></td></tr> | | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.551Å</td></tr> |
| <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">CALCOCO2, NDP52 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr> | | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene></td></tr> |
| <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4han FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4han OCA], [http://pdbe.org/4han PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4han RCSB], [http://www.ebi.ac.uk/pdbsum/4han PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4han ProSAT]</span></td></tr> | | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4han FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4han OCA], [https://pdbe.org/4han PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4han RCSB], [https://www.ebi.ac.uk/pdbsum/4han PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4han ProSAT]</span></td></tr> |
| </table> | | </table> |
| == Function == | | == Function == |
| [[http://www.uniprot.org/uniprot/LEG8_HUMAN LEG8_HUMAN]] Lectin with a marked preference for 3'-O-sialylated and 3'-O-sulfated glycans.<ref>PMID:21288902</ref> [[http://www.uniprot.org/uniprot/CACO2_HUMAN CACO2_HUMAN]] May play a role in ruffle formation and actin cytoskeleton organization. Seems to negatively regulate constitutive secretion.<ref>PMID:17635994</ref> | | [https://www.uniprot.org/uniprot/LEG8_HUMAN LEG8_HUMAN] Lectin with a marked preference for 3'-O-sialylated and 3'-O-sulfated glycans.<ref>PMID:21288902</ref> |
| <div style="background-color:#fffaf0;">
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| == Publication Abstract from PubMed ==
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| Infectious bacteria are cleared from mammalian cells by host autophagy in combination with other upstream cellular components, such as the autophagic receptor NDP52 and sugar receptor galectin-8. However, the detailed molecular basis of the interaction between these two receptors remains to be elucidated. Here, we report the biochemical characterization of both NDP52 and galectin-8 as well as the crystal structure of galectin-8 complexed with an NDP52 peptide. The unexpected observation of nicotinamide adenine dinucleotide located at the carbohydrate-binding site expands our knowledge of the sugar-binding specificity of galectin-8. The NDP52-galectin-8 complex structure explains the key determinants for recognition on both receptors and defines a special orientation of N- and C-terminal carbohydrate recognition domains of galectin-8. Dimeric NDP52 forms a ternary complex with two monomeric galectin-8 molecules as well as two LC3C molecules. These results lay the groundwork for understanding how host cells target bacterial pathogens for autophagy.
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| Structural basis for recognition of autophagic receptor NDP52 by the sugar receptor galectin-8.,Kim BW, Hong SB, Kim JH, Kwon do H, Song HK Nat Commun. 2013;4:1613. doi: 10.1038/ncomms2606. PMID:23511477<ref>PMID:23511477</ref>
| | ==See Also== |
| | | *[[Galectin 3D structures|Galectin 3D structures]] |
| From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
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| </div>
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| <div class="pdbe-citations 4han" style="background-color:#fffaf0;"></div>
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| == References == | | == References == |
| <references/> | | <references/> |
| __TOC__ | | __TOC__ |
| </StructureSection> | | </StructureSection> |
| [[Category: Human]] | | [[Category: Homo sapiens]] |
| [[Category: Hong, S B]] | | [[Category: Large Structures]] |
| [[Category: Kim, B W]] | | [[Category: Hong SB]] |
| [[Category: Kim, J H]] | | [[Category: Kim B-W]] |
| [[Category: Kwon, D H]] | | [[Category: Kim JH]] |
| [[Category: Song, H K]] | | [[Category: Kwon DH]] |
| [[Category: Autophagy]] | | [[Category: Song HK]] |
| [[Category: Autophagy adapter molecule]]
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| [[Category: Cytosol]]
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| [[Category: Innate immunity]]
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| [[Category: Nad binding]]
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| [[Category: Ndp52 peoptide binding]]
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| [[Category: Sugar binding protein]]
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